期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 24, 期 1, 页码 40-46出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3336
关键词
-
资金
- National Science Foundation of China [31270765]
- Key Research and Development Program of MOST [2016YFA0501100]
- Beijing Municipal Science & Technology Commission [Z161100000116034]
- US National Institutes of Health [CA168635, ES007061, ES015252]
The central step in eukaryotic homologous recombination (HR) is ATP-dependent DNA-strand exchange mediated by the Rad51 recombinase. In this process, Rad51 assembles on single-stranded DNA (ssDNA) and generates a helical filament that is able to search for and invade homologous double-stranded DNA (dsDNA), thus leading to strand separation and formation of new base pairs between the initiating ssDNA and the complementary strand within the duplex. Here, we used cryo-EM to solve the structures of human RAD51 in complex with DNA molecules, in presynaptic and postsynaptic states, at near-atomic resolution. Our structures reveal both conserved and distinct structural features of the human RAD51-DNA complexes compared with their prokaryotic counterpart. Notably, we also captured the structure of an arrested synaptic complex. Our results provide new insight into the molecular mechanisms of the DNA homology search and strand-exchange processes.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据